The ribosome-associated complex RAC serves in a relay that directs nascent chains to Ssb

The ribosome-associated complex (RAC), which contains the Hsp40 protein Zuo1 and the non-canonical Hsp70 protein Ssz1 forms a chaperone triad with the fungal-specific Hsp70 protein Ssb. Here the authors combine X-ray crystallography, crosslinking and biochemical experiments and present the structure...

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Autores principales:	Ying Zhang, Genís Valentín Gesé, Charlotte Conz, Karine Lapouge, Jürgen Kopp, Tina Wölfle, Sabine Rospert, Irmgard Sinning
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/e06ed860d300430596e39786410b21de
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spelling	oai:doaj.org-article:e06ed860d300430596e39786410b21de2021-12-02T14:40:51ZThe ribosome-associated complex RAC serves in a relay that directs nascent chains to Ssb10.1038/s41467-020-15313-w2041-1723https://doaj.org/article/e06ed860d300430596e39786410b21de2020-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-15313-whttps://doaj.org/toc/2041-1723The ribosome-associated complex (RAC), which contains the Hsp40 protein Zuo1 and the non-canonical Hsp70 protein Ssz1 forms a chaperone triad with the fungal-specific Hsp70 protein Ssb. Here the authors combine X-ray crystallography, crosslinking and biochemical experiments and present the structure of the Zuo1 N-terminus bound to Ssz1 and demonstrate that Ssz1 is an active chaperone for nascent chains.Ying ZhangGenís Valentín GeséCharlotte ConzKarine LapougeJürgen KoppTina WölfleSabine RospertIrmgard SinningNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Ying Zhang Genís Valentín Gesé Charlotte Conz Karine Lapouge Jürgen Kopp Tina Wölfle Sabine Rospert Irmgard Sinning The ribosome-associated complex RAC serves in a relay that directs nascent chains to Ssb
description	The ribosome-associated complex (RAC), which contains the Hsp40 protein Zuo1 and the non-canonical Hsp70 protein Ssz1 forms a chaperone triad with the fungal-specific Hsp70 protein Ssb. Here the authors combine X-ray crystallography, crosslinking and biochemical experiments and present the structure of the Zuo1 N-terminus bound to Ssz1 and demonstrate that Ssz1 is an active chaperone for nascent chains.
format	article
author	Ying Zhang Genís Valentín Gesé Charlotte Conz Karine Lapouge Jürgen Kopp Tina Wölfle Sabine Rospert Irmgard Sinning
author_facet	Ying Zhang Genís Valentín Gesé Charlotte Conz Karine Lapouge Jürgen Kopp Tina Wölfle Sabine Rospert Irmgard Sinning
author_sort	Ying Zhang
title	The ribosome-associated complex RAC serves in a relay that directs nascent chains to Ssb
title_short	The ribosome-associated complex RAC serves in a relay that directs nascent chains to Ssb
title_full	The ribosome-associated complex RAC serves in a relay that directs nascent chains to Ssb
title_fullStr	The ribosome-associated complex RAC serves in a relay that directs nascent chains to Ssb
title_full_unstemmed	The ribosome-associated complex RAC serves in a relay that directs nascent chains to Ssb
title_sort	ribosome-associated complex rac serves in a relay that directs nascent chains to ssb
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/e06ed860d300430596e39786410b21de
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The ribosome-associated complex RAC serves in a relay that directs nascent chains to Ssb

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